ID I2JNE6_9GAMM Unreviewed; 889 AA.
AC I2JNE6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN Name=pepN {ECO:0000313|EMBL:EIF44498.1};
GN ORFNames=DOK_03478 {ECO:0000313|EMBL:EIF44498.1};
OS gamma proteobacterium BDW918.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae.
OX NCBI_TaxID=1168065 {ECO:0000313|EMBL:EIF44498.1, ECO:0000313|Proteomes:UP000003473};
RN [1] {ECO:0000313|EMBL:EIF44498.1, ECO:0000313|Proteomes:UP000003473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BDW918 {ECO:0000313|EMBL:EIF44498.1,
RC ECO:0000313|Proteomes:UP000003473};
RX PubMed=22740675; DOI=10.1128/JB.00678-12;
RA Kim S.M., Cho S.J., Lee S.B.;
RT "Genome Sequence of the Unclassified Marine Gammaproteobacterium BDW918.";
RL J. Bacteriol. 194:3753-3754(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC amino acids including Pro (slow action). When a terminal hydrophobic
CC residue is followed by a prolyl residue, the two may be released as
CC an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIF44498.1}.
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DR EMBL; AJMK01000019; EIF44498.1; -; Genomic_DNA.
DR AlphaFoldDB; I2JNE6; -.
DR MEROPS; M01.005; -.
DR PATRIC; fig|1168065.3.peg.740; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_007993_2_0_6; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000003473; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09600; M1_APN; 1.
DR Gene3D; 2.60.40.1840; -; 1.
DR Gene3D; 3.30.2010.30; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 1.25.50.10; Peptidase M1, alanyl aminopeptidase, C-terminal domain; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR038438; PepN_Ig-like_sf.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR012779; Peptidase_M1_pepN.
DR InterPro; IPR024601; Peptidase_M1_pepN_C.
DR InterPro; IPR037144; Peptidase_M1_pepN_C_sf.
DR InterPro; IPR035414; Peptidase_M1_pepN_Ig-like.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02414; pepN_proteo; 1.
DR PANTHER; PTHR46322; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46322:SF1; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR Pfam; PF11940; DUF3458; 1.
DR Pfam; PF17432; DUF3458_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:EIF44498.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000003473};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 54..192
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 235..444
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 450..557
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 562..883
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 889 AA; 99060 MW; 0D3B1B19E79DA7BB CRC64;
MRDAQPSTIY LSEYQVPAYL IDTTALVFEL GEESTKVSSQ LHIRRNPAST ISNAPLALHG
TELELISLAI DGRTLDASEW TQSGEQLIIA SVPAEFVLSC ETRIRPQDNT SLEGLYKSSG
MFCTQCEAEG FRKITYYLDR PDVMSVFTVE IIADAQRYPV LLSNGNLSAA EVLADGRHKT
VWQDPFPKPA YLFALVAGKL ACVEDRFKTM SGRDVALKIY VEDKDADKCE HAMVSLKNAM
RWDEEVYGRE YDLDIFNIVA VDDFNMGAME NKSLNIFNTS CVLAKPETTT DAGFQRVEGV
VAHEYFHNWS GNRVTCRDWF QLSLKEGFTV FRDAEFSADM GSPTVKRVED VTLLRTAQFA
EDAGPMAHPI RPDSFIEISN FYTVTVYEKG AEVVRMIHTL LGPELFRKGS DLYFDRHDGQ
AVTCEDFVLA MEDASGVDLG QFRNWYSQAG TPKLKVSAEY DAAAQTYTLH VQQSCPATPG
QSKKAPFHIP FAVALLGEAG QLALQLQNAA LNTETADNTE MVLNVTKAEQ SFIFTGIKEE
PVPSLLRGFS APVKLEFDYS REQLLRLMSS DSDGFCRWDA SQQLGLAEIS QALADIAAEH
DVVPESAYLD ACRALLSDES LDGAMVAMML QLPSEAYLAE IFHPVDVLGL HRARETLRLV
IAQALRGELL ACYSRCASNA VYAADAGQIA QRSLKNTALS YLMLLNDDTG RELATRQFEH
SENMTDRLAA LNALVNSTAP YKAEALQRFY QNWQHEPLVI NQWFQVQAMC RLPGTLETVQ
GLMAHPAFDI RNPNKVRALI GAFCGQNSVN FHREDGAGYR FLADQVIVLN RSNPQIASRL
LVPLTKWRKY LPAAQQLMCA ELQRILAQPD LSSDVYEVVS KSVQEYSEE
//
